| Identification |
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| Name: | 2-octaprenyl-6-methoxyphenol hydroxylase |
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| Synonyms: | Not Available |
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| Gene Name: | ubiH |
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| Enzyme Class: | Not Available |
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| Biological Properties |
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| General Function: | Involved in oxidoreductase activity |
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| Specific Function: | Oxygenase that introduces the hydroxyl group at carbon four of 2-octaprenyl-6-methoxyphenol resulting in the formation of 2-octaprenyl-6-methoxy-1,4-benzoquinone |
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| Cellular Location: | Not Available |
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| SMPDB Pathways: | - Secondary Metabolites: Ubiquinol biosynthesis PW000981
- Secondary Metabolites: Ubiquinol biosynthesis 2 PW002036
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| KEGG Pathways: | - Ubiquinone and other terpenoid-quinone biosynthesis ec00130
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| KEGG Reactions: | |
1.02-Polyprenyl-6-methoxyphenol | + | 1.0 | ↔ | 1.02-Polyprenyl-6-methoxy-1,4-benzoquinone | + | 1.0 |
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| SMPDB Reactions: | |
1.0 | + | 1.0NADPH | + | 1.0 | + | 1.0 | + | 1.0 | → | 1.0 | + | 1.0 | + | 1.0 |
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| EcoCyc Reactions: | |
1.0 | + | 1.0 | + | 1.0 | + | 1.0 | → | 1.0 | + | 1.0 | + | 1.0 |
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| Complex Reactions: | |
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| Metabolites: | |
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| GO Classification: | | Function |
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| adenyl nucleotide binding | | binding | | catalytic activity | | FAD or FADH2 binding | | monooxygenase activity | | nucleoside binding | | oxidoreductase activity | | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NADH or NADPH as one donor, and incorporation of one atom of oxygen | | purine nucleoside binding | | Process |
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| cellular metabolic process | | coenzyme metabolic process | | cofactor metabolic process | | metabolic process | | oxidation reduction | | oxidoreduction coenzyme metabolic process | | ubiquinone biosynthetic process | | ubiquinone metabolic process |
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| Gene Properties |
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| Blattner: | b2907 |
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| Gene Orientation | Counterclockwise |
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| Centisome Percentage: | 65.75 |
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| Left Sequence End | 3050362 |
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| Right Sequence End | 3051540 |
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| Gene Sequence: | >1179 bp
ATGATCTGGATAATGACGATGGCTCGCCGTATGAACGGTGTTTACGCGGCATTTATGCTG
GTCGCTTTTATGATGGGGGTGGCCGGGGCGCTACAGGCTCCTACATTGAGCTTATTTCTG
AGTCGTGAGGTTGGCGCGCAACCTTTCTGGATCGGCCTCTTTTATACGGTGAATGCTATT
GCTGGGATCGGCGTAAGCCTCTGGTTGGCAAAACGTTCTGACAGTCAGGGCGATCGGCGA
AAACTGATTATATTTTGCTGTTTGATGGCTATCGGCAATGCGCTATTGTTTGCATTTAAT
CGTCATTATCTGACGCTTATCACCTGTGGTGTGCTTCTGGCATCTCTGGCCAATACGGCA
ATGCCACAGTTATTTGCTCTGGCGCGGGAATATGCGGATAACTCGGCGCGAGAAGTGGTG
ATGTTTAGCTCGGTGATGCGTGCGCAGCTTTCTCTGGCATGGGTTATCGGTCCACCGTTG
GCCTTTATGCTGGCGTTGAATTACGGCTTTACGGTGATGTTTTCGATTGCCGCCGGGATA
TTCACACTCAGTCTGGTATTGATTGCATTTATGCTTCCGTCTGTGGCGCGGGTAGAACTG
CCGTCGGAAAATGCTTTATCAATGCAAGGTGGCTGGCAGGATAGTAACGTACGGATGTTA
TTTGTCGCCTCGACGTTAATGTGGACCTGCAACACCATGTACATTATTGATATGCCGTTG
TGGATCAGTAGCGAGTTAGGATTGCCAGACAAACTGGCGGGTTTCCTGATGGGGACGGCA
GCTGGACTGGAAATACCAGCAATGATTCTGGCTGGCTACTATGTCAAACGTTATGGTAAG
CGGCGAATGATGGTCATAGCAGTGGCGGCAGGAGTACTGTTTTACACCGGATTGATTTTC
TTTAATAGCCGTATGGCGTTGATGACGCTGCAACTTTTTAACGCTGTATTTATCGGCATT
GTTGCGGGTATTGGGATGCTATGGTTTCAGGATTTAATGCCTGGAAGAGCGGGGGCAGCT
ACCACCTTATTTACTAACAGTATTTCTACCGGGGTAATTCTGGCTGGCGTTATTCAGGGA
GCAATTGCACAAAGTTGGGGGCACTTTGCTGTCTACTGGGTAATTGCGGTTATTTCTGTT
GTCGCATTATTTTTAACCGCAAAGGTTAAAGACGTTTGA |
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| Protein Properties |
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| Pfam Domain Function: | |
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| Protein Residues: | 392 |
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| Protein Molecular Weight: | 42288 |
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| Protein Theoretical pI: | 7 |
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| Signaling Regions: | |
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| Transmembrane Regions: | |
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| Protein Sequence: | >2-octaprenyl-6-methoxyphenol hydroxylase
MSVIIVGGGMAGATLALAISRLSHGALPVHLIEATAPESHAHPGFDGRAIALAAGTCQQL
ARIGVWQSLADCATAITTVHVSDRGHAGFVTLAAEDYQLAALGQVVELHNVGQRLFALLR
KAPGVTLHCPDRVANVARTQSHVEVTLESGETLTGRVLVAADGTHSALATACGVDWQQEP
YEQLAVIANVATSVAHEGRAFERFTQHGPLAMLPMSDGRCSLVWCHPLERREEVLSWSDE
KFCRELQSAFGWRLGKITHAGKRSAYPLALTHAARSITHRTVLVGNAAQTLHPIAGQGFN
LGMRDVMSLAETLTQAQERGEDMGDYGVLCRYQQRRQSDREATIGVTDSLVHLFANRWAP
LVVGRNIGLMTMELFTPARDVLAQRTLGWVAR |
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| References |
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| External Links: | |
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| General Reference: | - Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
- Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
- Nakahigashi, K., Miyamoto, K., Nishimura, K., Inokuchi, H. (1992). "Isolation and characterization of a light-sensitive mutant of Escherichia coli K-12 with a mutation in a gene that is required for the biosynthesis of ubiquinone." J Bacteriol 174:7352-7359. Pubmed: 1339425
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